ArticleeLife2016
Structural elucidation of a novel mechanism for the bacteriophage-based inhibition of the RNA degradosome.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
39 citing papers in PubMed, 59 citations in OpenAlex.
- Article
- The biology of jumbo phages.Nature communications · 2026Review
- Bacteriophage deploys a RecA-dependent nuclease to inhibit Staphylococcus aureus replication and promote phage propagation.Nucleic acids research · 2026Article
- Bacteriophage genome-wide transposon mutagenesis.bioRxiv : the preprint server for biology · 2025Article
- The ribonuclease E regulator RebA is essential for diazotrophic growth in the cyanobacteriummLife · 2025Article
- Critical functions and key interactions mediated by the RNase E scaffolding domain in Pseudomonas aeruginosa.PLoS genetics · 2025Article
- Genome-wide identification of bacterial genes contributing to nucleus-forming jumbo phage infection.Nucleic acids research · 2025Article
- Phage proteins target and co-opt host ribosomes immediately upon infection.Nature microbiology · 2024Article
- A conserved protein inhibitor brings under check the activity of RNase E in cyanobacteria.Nucleic acids research · 2024Article
- The Dynamics of Synthesis and Localization of Jumbo Phage RNA Polymerases inside Infected Cells.Viruses · 2023Article
- Next-generation proteomics for quantitative Jumbophage-bacteria interaction mapping.Nature communications · 2023Article
- Significant Differences in Planktonic Virus Communities Between "Cellular Fraction" (0.22 ~ 3.0 µm) and "Viral Fraction" (< 0.22 μm) in the Ocean.Microbial ecology · 2023Article
- Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation.International journal of molecular sciences · 2022Article
- The world of ribonucleases from pseudomonads: a short trip through the main features and singularities.Microbial biotechnology · 2021Review
- Article
- The DEAD-box RNA helicase RhlE2 is a global regulator of Pseudomonas aeruginosa lifestyle and pathogenesis.Nucleic acids research · 2021Article
- Trans-acting regulators of ribonuclease activity.Journal of microbiology (Seoul, Korea) · 2021Review
- Article
- Phase-separated bacterial ribonucleoprotein bodies organize mRNA decay.Wiley interdisciplinary reviews. RNA · 2020Review
- Exploring the synthetic biology potential of bacteriophages for engineering non-model bacteria.Nature communications · 2020Review
Corrections and comments
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
In all domains of life, the catalysed degradation of RNA facilitates rapid adaptation to changing environmental conditions, while destruction of foreign RNA is an important mechanism to prevent host infection. We have identified a virus-encoded protein termed gp37/Dip, which directly binds and inhibits the RNA degradation machinery of its bacterial host. Encoded by giant phage фKZ, this protein associates with two RNA binding sites of the RNase E component of the Pseudomonas aeruginosa RNA degradosome, occluding them from substrates and resulting in effective inhibition of RNA degradation and processing. The 2.2 Å crystal structure reveals that this novel homo-dimeric protein has no identifiable structural homologues. Our biochemical data indicate that acidic patches on the convex outer surface bind RNase E. Through the activity of Dip, фKZ has evolved a unique mechanism to down regulate a key metabolic process of its host to allow accumulation of viral RNA in infected cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.